1b0p: Difference between revisions

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[[Image:1b0p.~~gif~~|left|200px]]

[[Image:1b0p.png|left|200px]]

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~~'''~~CRYSTAL STRUCTURE OF PYRUVATE-FERREDOXIN OXIDOREDUCTASE FROM DESULFOVIBRIO AFRICANUS~~'''~~

===CRYSTAL STRUCTURE OF PYRUVATE-FERREDOXIN OXIDOREDUCTASE FROM DESULFOVIBRIO AFRICANUS===

~~==Overview==~~

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~~Oxidative decarboxylation of pyruvate to form acetyl-coenzyme A~~, ~~a crucial step in many metabolic pathways~~, ~~is carried out in most aerobic organisms by~~ the ~~multienzyme complex pyruvate dehydrogenase. In most anaerobes,~~ the ~~same reaction is usually catalyzed by a single enzyme, pyruvate~~:~~ferredoxin oxidoreductase (PFOR~~)~~. Thus~~, ~~PFOR~~ is ~~a potential target for drug design against certain anaerobic pathogens. Here, we report~~ the ~~crystal structures of the homodimeric Desulfovibrio africanus PFOR (data to 2~~.3 A resolution), and of its complex with pyruvate (3.0 A resolution). The structures show that each subunit consists of seven domains, one of which affords protection against oxygen. The thiamin pyrophosphate (TPP) cofactor and the three [4Fe-~~4S] clusters are suitably arranged to provide a plausible electron transfer pathway. In addition, the PFOR~~-~~pyruvate complex structure shows the noncovalent fixation of the substrate before the catalytic reaction.~~

The line below this paragraph, {{ABSTRACT_PUBMED_10048931}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10048931 is the PubMed ID number.

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==About this Structure==

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[[Category: Pyruvate catabolism]]

[[Category: Tpp-dependent enzyme]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 10~~:55:38 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:59:47 2008''

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-[[Image:1b0p.gif|left|200px]]
+{{Seed}}
+[[Image:1b0p.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1b0p|  PDB=1b0p  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF PYRUVATE-FERREDOXIN OXIDOREDUCTASE FROM DESULFOVIBRIO AFRICANUS'''
+===CRYSTAL STRUCTURE OF PYRUVATE-FERREDOXIN OXIDOREDUCTASE FROM DESULFOVIBRIO AFRICANUS===
-==Overview==
+<!--
-Oxidative decarboxylation of pyruvate to form acetyl-coenzyme A, a crucial step in many metabolic pathways, is carried out in most aerobic organisms by the multienzyme complex pyruvate dehydrogenase. In most anaerobes, the same reaction is usually catalyzed by a single enzyme, pyruvate:ferredoxin oxidoreductase (PFOR). Thus, PFOR is a potential target for drug design against certain anaerobic pathogens. Here, we report the crystal structures of the homodimeric Desulfovibrio africanus PFOR (data to 2.3 A resolution), and of its complex with pyruvate (3.0 A resolution). The structures show that each subunit consists of seven domains, one of which affords protection against oxygen. The thiamin pyrophosphate (TPP) cofactor and the three [4Fe-4S] clusters are suitably arranged to provide a plausible electron transfer pathway. In addition, the PFOR-pyruvate complex structure shows the noncovalent fixation of the substrate before the catalytic reaction.
+The line below this paragraph, {{ABSTRACT_PUBMED_10048931}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10048931 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10048931}}
 ==About this Structure==
@@ Line 30: / Line 34: @@
 [[Category: Pyruvate catabolism]]
 [[Category: Tpp-dependent enzyme]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:55:38 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:59:47 2008''